Journal
JOURNAL OF CELL BIOLOGY
Volume 183, Issue 7, Pages 1275-1286Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200806062
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Funding
- Solution Oriented Research for Science and Technology and Core Research for Evolutional Science and Technology
- Science and Technology Agency of Japan
- National Project on Protein Structural and Functional Analyses
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Japan Foundation for Applied Enzymology
- Takeda Foundation for Biomedical Research
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Two distinct pathways have recently been proposed for the import of peroxisomal membrane proteins (PMPs): a Pex19p- and Pex3p-dependent class I pathway and a Pex19p- and Pex3p-independent class II pathway. We show here that Pex19p plays an essential role as the chaperone for full-length Pex3p in the cytosol. Pex19p forms a soluble complex with newly synthesized Pex3p in the cytosol and directly translocates it to peroxisomes. Knockdown of Pex19p inhibits peroxisomal targeting of newly synthesized full-length Pex3p and results in failure of the peroxisomal localization of Pex3p. Moreover, we demonstrate that Pex16p functions as the Pex3p-docking site and serves as the peroxisomal membrane receptor that is specific to the Pex3p-Pex19p complexes. Based on these novel. findings, we suggest a model for the import of PMPs that provides new insights into the molecular mechanisms underlying the biogenesis of peroxisomes and its regulation involving Pex3p, Pex19p, and Pex16p.
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